The immobilization of proteins on the surface of carriers is challenging due to the loss of protein structure and function in this process. Here, we report the development of the protein immobilization on the surface of the metallated‐porphyrin complex in the porphysome nanocarrier. The conjugated Ni‐porphyrin to fatty acid (as a tail) has been synthesized and independently placed at the depth of the bilayer center of Dipalmitoylphosphatidylcholine (DPPC) in which the Ni‐porphyrin was at the polar region of the membrane and is thus superficial. This porphysome (DPPC: Ni‐porphyrin, 4:1 mole ratio) was formed by supramolecular self‐assembly with a diameter of 173±7 nm and zeta potential ‐8.5±3.4 mv, which exhibited no significant toxicity at the experimental concentrations and acceptable cellular uptake on MCF‐7 cells. The physicochemical properties and specific protein binding sites of the firefly luciferase as a model protein into the porphysome (1:2 mole ratio) show the conjugation efficiency about 80% and the conformation of protein was completely maintained. Furthermore, bioluminescence assay and SDS‐PAGE confirmed the preservation of protein function. The stabilized platform of porphyrin‐lipid structure can potentially improve the efficacy of protein functionality for a particular display, shifting porphysomes from a simple carrier to a therapeutic agent.

中文翻译：

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具有特定蛋白质结合位点的卟啉体作为用于靶向蛋白质递送的多模式治疗诊断纳米载体

由于在此过程中蛋白质结构和功能的损失，将蛋白质固定在载体表面具有挑战性。在这里，我们报告了卟啉体纳米载体中金属化卟啉复合物表面蛋白质固定化的进展。已合成了与脂肪酸共轭的镍卟啉（作为尾部），并独立放置在二棕榈酰磷脂酰胆碱（DPPC）双层中心的深处，其中镍卟啉位于膜的极性区域，因此处于表面。该卟啉体（DPPC：镍卟啉，摩尔比为4：1）由超分子自组装形成，直径为173±7 nm，zeta电位为‐8.5±3.4 mv，在实验浓度下没有表现出明显的毒性，可以接受。 MCF-7 细胞的细胞摄取。以萤火虫荧光素酶为模型蛋白进入卟啉体（1:2摩尔比）的理化性质和特异性蛋白结合位点显示结合效率约为80%，并且蛋白构象完全保持。此外，生物发光测定和 SDS-PAGE 证实了蛋白质功能的保存。卟啉-脂质结构的稳定平台可以潜在地提高特定显示的蛋白质功能的功效，将卟啉体从简单的载体转变为治疗剂。